Achim Recktenwald, PhD wrote:
>> We want to change the surface hydrophobicity of several proteins through
> chemical modifications.
>> My problem now is to find a method which allows me to measure the
> protein's hydrophobicity and the changes achieved. So far, the best
> solution I could come up with is to perform reversed-phase
> chromatography. I would use the elution-shift during the gradient from
> aqueous to organic solvent as a value for the change in hydrophobicity.
>> But I assume, I am not the first one to have this problem. Any better
> methods available ?
>> Thanks for any hint.
>> Achim
>> P.S. Please email me an answer, as well (achim at ibex.ca); our
> service-provider has too often problems with the usenet-server.
>> _____________________________
> Achim Recktenwald, PhD
> IBEX Technologies, Inc.
> 5485 rue Pare
> Montreal, PQ, H4P 1P7
> Canada
>> Phone: (514) 344-4004
> Fax : (514) 344-8827
> email: achim at ibex.ca
You could try ANS fluorescence studies. This dye (anilino naphthalene
sulfate, I think is its full name) binds to hydrophobic patches on the
protein surface, on doing so a measurable fluorescence change occurs in
its emittance. I have seen several papers which have used this method to
determine protein hydrophobicity. Perhaps a medline search would turn up
the relevant details.
Hope this helps,
Len Bell.
University of Liverpool. Uk
lgbell at liv.ac.uk